Analysis of the site-specific asparagine-linked glycosylation of recombinant human coagulation factor VIIa by glycosidase digestions, liquid chromatography, and mass spectrometry.

Abstract:

:The two asparagine-linked glycosylation sites of recombinant coagulation factor VIIa have been characterized by glycosidase digestions, size-exclusion chromatography (SEC), and mass spectrometry (MS). Nine structures were characterized as core fucosylated bi-and triantennary structures with 0-3 sialic-acid residues which were alpha 2-3 linked to galactose exclusively. Three of the structures had one or two galactose residues substituted by N-acetylgalactosamine. Significant differences were found between the oligosaccharide profiles for the two glycosylation sites in rFVIIa. At Asn322, the degree of sialylation was lower and higher amounts of structures containing N-acetylgalactosamine were found compared to Asn145.

journal_name

Mol Biotechnol

journal_title

Molecular biotechnology

authors

Klausen NK,Bayne S,Palm L

subject

Has Abstract

pub_date

1998-06-01 00:00:00

pages

195-204

issue

3

eissn

1073-6085

issn

1559-0305

journal_volume

9

pub_type

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